2hbs
From Proteopedia
THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S
Overview
We have refined the crystal structure of deoxyhemoglobin S (beta Glu6-->Val) at 2.05 A resolution to an R-factor of 16.5% (free R=21. 5%) using crystals isomorphous to those originally grown by Wishner and Love. A predominant feature of this crystal form is a double strand of hemoglobin tetramers that has been shown by a variety of techniques to be the fundamental building block of the intracellular sickle cell fiber. The double strand is stabilized by lateral contacts involving the mutant valine interacting with a pocket between the E and F helices on another tetramer. The new structure reveals some marked differences from the previously refined 3.0 A resolution structure, including several residues in the lateral contact which have shifted by as much as 3.5 A. The lateral contact includes, in addition to the hydrophobic interactions involving the mutant valine, hydrophilic interactions and bridging water molecules at the periphery of the contact. This structure provides further insights into hemoglobin polymerization and may be useful for the structure-based design of therapeutic agents to treat sickle cell disease.
About this Structure
2HBS is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 2HBS with [Hemoglobin]. Full crystallographic information is available from OCA.
Reference
The high resolution crystal structure of deoxyhemoglobin S., Harrington DJ, Adachi K, Royer WE Jr, J Mol Biol. 1997 Sep 26;272(3):398-407. PMID:9325099 Page seeded by OCA on Mon May 26 21:55:23 2008
